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Related Concept Videos

Noncovalent Attractions in Biomolecules02:35

Noncovalent Attractions in Biomolecules

Noncovalent attractions are associations within and between molecules that influence the shape and structural stability of complexes. These interactions differ from covalent bonding in that they do not involve sharing of electrons.
Four types of noncovalent interactions are hydrogen bonds, van der Waals forces, ionic bonds, and hydrophobic interactions.
Hydrogen bonding results from the electrostatic attraction of a hydrogen atom covalently bonded to a strong-electronegative atom like oxygen,...
Noncovalent Attractions in Biomolecules02:35

Noncovalent Attractions in Biomolecules

Noncovalent attractions are associations within and between molecules that influence the shape and structural stability of complexes. These interactions differ from covalent bonding in that they do not involve sharing of electrons.
Four types of noncovalent interactions are hydrogen bonds, van der Waals forces, ionic bonds, and hydrophobic interactions.
Hydrogen bonding results from the electrostatic attraction of a hydrogen atom covalently bonded to a strong-electronegative atom like oxygen,...
Van der Waals Interactions01:24

Van der Waals Interactions

Atoms and molecules interact with each other through intermolecular forces. These electrostatic forces arise from attractive or repulsive interactions between particles with permanent, partial, or temporary charges. The intermolecular forces between neutral atoms and molecules are ion–dipole, dipole–dipole, and dispersion forces, collectively known as van der Waals forces.Polar molecules have a partial positive charge on one end and a partial negative charge on the other end of the molecule,...
Drug-Receptor Bonds01:25

Drug-Receptor Bonds

Drug-receptor bonds are formed through various chemical forces when drugs interact with target cells. Covalent bonds, strong and irreversible, are exemplified by DNA-alkylating anticancer agents that inhibit cell division. However, such irreversible drug binding lacks selectivity and can modify the DNA of the surrounding healthy cells. Covalent binding often contributes to tissue toxicity, as seen with chloroform and paracetamol metabolites binding to the liver, causing hepatotoxicity.
In...
Intermolecular Forces03:13

Intermolecular Forces

Atoms and molecules interact through bonds (or forces): intramolecular and intermolecular. The forces are electrostatic as they arise from interactions (attractive or repulsive) between charged species (permanent, partial, or temporary charges) and exist with varying strengths between ions, polar, nonpolar, and neutral molecules. The different types of intermolecular forces are ion–dipole, dipole–dipole, hydrogen bonds, and dispersion; among these, dipole–dipole, hydrogen bonds, and dispersion...
Intermolecular Forces03:13

Intermolecular Forces

Atoms and molecules interact through bonds (or forces): intramolecular and intermolecular. The forces are electrostatic as they arise from interactions (attractive or repulsive) between charged species (permanent, partial, or temporary charges) and exist with varying strengths between ions, polar, nonpolar, and neutral molecules. The different types of intermolecular forces are ion–dipole, dipole–dipole, hydrogen bonds, and dispersion; among these, dipole–dipole, hydrogen bonds, and dispersion...

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Exploring Protein-Glycan Interactions: Advances in Nuclear Magnetic Resonance
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Non-covalent interactions in biomacromolecules.

Jirí Cerný1, Pavel Hobza

  • 1Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic.

Physical Chemistry Chemical Physics : PCCP
|October 5, 2007
PubMed
Summary

Non-covalent interactions are crucial for biomolecular structures like DNA and proteins. Accurate calculation of these interaction energies, including hydrogen bonding and dispersion forces, is essential for understanding molecular recognition.

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Area of Science:

  • Biochemistry and Molecular Biology
  • Computational Chemistry

Background:

  • Non-covalent interactions are fundamental to the structure and function of biomacromolecules, including DNA and proteins.
  • These interactions are critical for molecular recognition processes in biological systems.

Purpose of the Study:

  • To review methods for theoretical evaluation of non-covalent interaction energies.
  • To highlight the importance of accurate energy calculations for understanding biomolecular stability and recognition.

Main Methods:

  • Brief description of perturbation and variation (supermolecular) methods for calculating interaction energies.
  • Emphasis on complete basis set limit calculations, including coupled cluster methods like CCSD(T), for accurate results.
  • Discussion of the role of hydrogen bonding, stacking interactions, and London dispersion energy.

Main Results:

  • Accurate calculation of interaction energies requires covering a significant portion of the correlation energy.
  • Hydrogen bonding and stacking interactions are key stabilizing forces in DNA, oligopeptides, and proteins.
  • London dispersion energy plays a significant role in the overall stabilization.

Conclusions:

  • Theoretical evaluation of non-covalent interactions is challenging but achievable with advanced computational methods.
  • Understanding these interactions is vital for fields ranging from chemistry to biodisciplines.
  • Accurate computational models are essential for predicting and understanding biomolecular behavior.